NCERT Solutions for Class 11th Biology
Chapter 9 Biomolecules
1. What are macromolecules ? Give examples.
Solution: Macromolecules are large high molecular weight substances with complex molecular structure and occur in colloidal state (being insoluble) in intracellular fluid. These are formed by polymerisation of large number of micromolecules. Polysaccharides, proteins and nucleic acids are few examples.
Solution: Macromolecules are large high molecular weight substances with complex molecular structure and occur in colloidal state (being insoluble) in intracellular fluid. These are formed by polymerisation of large number of micromolecules. Polysaccharides, proteins and nucleic acids are few examples.
2. Illustrate a glycosidic, peptide, and a phospho- diester bond.
Solution. (i) Glycosidic bond is the type of chemical linkage between the monosaccharide units of disaccharides, oligosaccharides and polysaccharides, which is formed by the removal of a molecule of water.
(ii)Peptide bonds are formed by the reaction between carboxyl (- COOH) of one amino acid and amino (- NH2) group of other amino acid with the elimination of water.
(iii) In a polynucleotide chain, adjacent nucleotides are joined together by a bond called phosphodiester bond. This bond links a phosphate group and sugar group of two adjacent nucleotides by means of an oxygen bridge.
Solution. (i) Glycosidic bond is the type of chemical linkage between the monosaccharide units of disaccharides, oligosaccharides and polysaccharides, which is formed by the removal of a molecule of water.
(ii)Peptide bonds are formed by the reaction between carboxyl (- COOH) of one amino acid and amino (- NH2) group of other amino acid with the elimination of water.
(iii) In a polynucleotide chain, adjacent nucleotides are joined together by a bond called phosphodiester bond. This bond links a phosphate group and sugar group of two adjacent nucleotides by means of an oxygen bridge.
3. What is meant by tertiary structure of proteins?
Solution: The helical polypeptide molecule may fold on itself and assume a complex but specific form-spherical, rod-like or any form in between these. These geometrical shapes,are known as tertiary (3°) structure of protein molecules. The coils and folds of the polypeptide molecules are so arranged as to hide the non-polar amino acid chains inside and to expose the polar side chains. The tertiary structure of a protein brings distant amino acid side chains nearer to form active sites of enzymatic proteins. The tertiary structure is maintained by weak bonds such as hydrogen, ionic, disulphide and hydrophilic – hydrophobic bonds, formed between one part of a polypeptide and another. This structure is easily disrupted by pH, temperature and chemicals stopping the function of proteins.
Solution: The helical polypeptide molecule may fold on itself and assume a complex but specific form-spherical, rod-like or any form in between these. These geometrical shapes,are known as tertiary (3°) structure of protein molecules. The coils and folds of the polypeptide molecules are so arranged as to hide the non-polar amino acid chains inside and to expose the polar side chains. The tertiary structure of a protein brings distant amino acid side chains nearer to form active sites of enzymatic proteins. The tertiary structure is maintained by weak bonds such as hydrogen, ionic, disulphide and hydrophilic – hydrophobic bonds, formed between one part of a polypeptide and another. This structure is easily disrupted by pH, temperature and chemicals stopping the function of proteins.
4. Find and write down structures ©f 10 interesting small molecular weight biomolecules.
Solution: Interesfing small molecular weight biomolecules are minerals (like sodium, potassium, calcium, zinc, iodine etc), gases (like Oz, N2, C02, NH3) sugars – (ribose, deoxyribose, glucose, fructose), lipids, amino acids, nucleotides (pyrimidines & purine). Structures of 10 interesting small molecular weight biomolecules are as follows:
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Solution: Interesfing small molecular weight biomolecules are minerals (like sodium, potassium, calcium, zinc, iodine etc), gases (like Oz, N2, C02, NH3) sugars – (ribose, deoxyribose, glucose, fructose), lipids, amino acids, nucleotides (pyrimidines & purine). Structures of 10 interesting small molecular weight biomolecules are as follows:
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Question 5: Proteins have primary structure. If you are given a method to know which amino acid is at either of the two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein?
Answer Yes, if we are given a method to know the sequence of proteins, we can connect this information to the purity of a protein. It is known that an accurate sequence of a certain amino acid is very important for the functioning of a protein. If there is any change in the sequence, it would alter its structure, thereby altering the function. If
we are provided with a method to know the sequence of an unknown protein, then using this information, we can determine its structure and compare it with any of the known correct protein sequence. Any change in the sequence can be linked to the purity or homogeneity of a protein.
For example, any one change in the sequence of haemoglobin can alter the normal haemoglobin structure to an abnormal structure that can cause sickle cell anaemia.
Answer Yes, if we are given a method to know the sequence of proteins, we can connect this information to the purity of a protein. It is known that an accurate sequence of a certain amino acid is very important for the functioning of a protein. If there is any change in the sequence, it would alter its structure, thereby altering the function. If
we are provided with a method to know the sequence of an unknown protein, then using this information, we can determine its structure and compare it with any of the known correct protein sequence. Any change in the sequence can be linked to the purity or homogeneity of a protein.
For example, any one change in the sequence of haemoglobin can alter the normal haemoglobin structure to an abnormal structure that can cause sickle cell anaemia.
Question 6: Find out and make a list of proteins used as therapeutic agents. Find other applications of proteins (e.g., cosmetics, etc.)
Answer Proteins used as therapeutic agents are as follows:
1. Thrombin and fibrinogen – They help in blood clotting.
2. Antigen (antibody) – It helps in blood transfusion.
3. Insulin – It helps in maintaining blood glucose level in the body.
4. Renin – It helps in osmoregulation.
Proteins are also commonly used in the manufacture of cosmetics, toxins, and as biological buffers.
Answer Proteins used as therapeutic agents are as follows:
1. Thrombin and fibrinogen – They help in blood clotting.
2. Antigen (antibody) – It helps in blood transfusion.
3. Insulin – It helps in maintaining blood glucose level in the body.
4. Renin – It helps in osmoregulation.
Proteins are also commonly used in the manufacture of cosmetics, toxins, and as biological buffers.
Question 7: Explain the composition of triglyceride.
Answer Triglyceride is a glyceride, which is formed from a single molecule of glycerol, esterified with three fatty acids. It is mainly present in vegetable oils and animal fat.
Answer Triglyceride is a glyceride, which is formed from a single molecule of glycerol, esterified with three fatty acids. It is mainly present in vegetable oils and animal fat.
Question 8: Can you describe what happens when milk is converted into curd or yoghurt from your understanding of proteins.
Answer Proteins are macromolecules formed by the polymerization of amino acids. Structurally, proteins are divided into four levels.
(a) Primary structure – It is the linear sequence of amino acids in a polypeptide chain.
(b) Secondary structure – The polypeptide chain is coiled to form a threedimensional structure.
(c) Tertiary structure – The helical polypeptide chain is further coiled and folded to form a complex structure.
(d) Quaternary structure – More than one polypeptide chains assemble to form the quaternary structure.
Milk has many globular proteins. When milk is converted into curd or yoghurt, these complex proteins get denatured, thus converting globular proteins into fibrous proteins. Therefore, by the process of denaturation, the secondary and tertiary structures of proteins are destroyed.
Answer Proteins are macromolecules formed by the polymerization of amino acids. Structurally, proteins are divided into four levels.
(a) Primary structure – It is the linear sequence of amino acids in a polypeptide chain.
(b) Secondary structure – The polypeptide chain is coiled to form a threedimensional structure.
(c) Tertiary structure – The helical polypeptide chain is further coiled and folded to form a complex structure.
(d) Quaternary structure – More than one polypeptide chains assemble to form the quaternary structure.
Milk has many globular proteins. When milk is converted into curd or yoghurt, these complex proteins get denatured, thus converting globular proteins into fibrous proteins. Therefore, by the process of denaturation, the secondary and tertiary structures of proteins are destroyed.
9. Can you attempt building models of biomolecules using commercially available atomic models (Ball and stick models).
Solution: Yes, models of biomolecules can be prepared using commercially available atomic models.
Ball and stick models and space filling models are 3D or spatial molecular models which serve to display the structure of chemical products and substances or biomolecules. With ball and stick models, the centers of the atoms are connected by straight lines which represent the covalent bonds. Double and triple bonds are often represented by springs which form curved connections between the balls. The bond angles and bond lengths reflect the actual relationships, while the space occupied by the atoms is either not represented at all or only denoted essentially by the relative sizes of the spheres.
Solution: Yes, models of biomolecules can be prepared using commercially available atomic models.
Ball and stick models and space filling models are 3D or spatial molecular models which serve to display the structure of chemical products and substances or biomolecules. With ball and stick models, the centers of the atoms are connected by straight lines which represent the covalent bonds. Double and triple bonds are often represented by springs which form curved connections between the balls. The bond angles and bond lengths reflect the actual relationships, while the space occupied by the atoms is either not represented at all or only denoted essentially by the relative sizes of the spheres.
10. Attempt titrating an amino acid against a weak base and discover the number of dissociating (ionizable) functional groups in the amino acid.
Solution: The existence of different ionic forms of amino acids can be easily understood by the titration curves. The number of dissociating functional group is one in case of neutral and basic amino acids and two in case of acidic amino acids.
Solution: The existence of different ionic forms of amino acids can be easily understood by the titration curves. The number of dissociating functional group is one in case of neutral and basic amino acids and two in case of acidic amino acids.
11. Draw the structure of the amino acid, alanine.
Solution:
Solution:
12. What are gums made of ? Is fevicol different ?
Solution: Gums are hetero-polysaccharides (poly-mers) of large number of different monosac-charide units. Yes, fevicol is a different kind of polymer. It is a synthetic sticky substance called resin which is manufactured by esteri-fication of organic compounds.
Solution: Gums are hetero-polysaccharides (poly-mers) of large number of different monosac-charide units. Yes, fevicol is a different kind of polymer. It is a synthetic sticky substance called resin which is manufactured by esteri-fication of organic compounds.
13. Find out a qualitative test for proteins, fats and oils, amino acids and test, any fruit juice, saliva, and urine for them.
Solution: Biuret test for protein : The biuret test is a chemical test used for determining the presence of peptide bonds. In a positive test, a copper II ion (Cu2+ ion) is reduced to copper I (Cu+) which forms a complex with the nitrogen and carbon of peptide bonds in an alkaline solution. A violet colour indicates the presence of proteins.
Ninhydrin test for amino acid: Ninhydrin (2,2 Dihydroxy indane-l,3-dione) is a chemical used to detect ammonia or primary and secondary amines. When reacting with these free amines, a deep blue or purple colour known as Ruhemann’s purple is evolved. Amino acid analysis of proteins is also done by ninhydrine. Most of the amino acids (including a-amino acids) are hydrolysed and reacted with ninhydrin except proline (a secondary amine). Amino acid containing a free amino group and a free carboxylic acid group reacts together with ninhydrin to produce coloured product. When the amino group is secondary, the condensation product is yellow.
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Solubility test for fats and oils : A positive solubility test for fats is that the fat dissolves in lighter fluid and not in water. In this test, 5 drops of fat or oil are added in two test tubes containing 10 drops of lighter fluid and 10 drops cold water respectively.
Fruit juice contains sugar so it cannot be tested by the above mentioned tests. Saliva contains proteins, mineral salts, amylase etc., so it can be tested for protein and amino acids. Urine contains proteins, so it can be tested for it.
Solution: Biuret test for protein : The biuret test is a chemical test used for determining the presence of peptide bonds. In a positive test, a copper II ion (Cu2+ ion) is reduced to copper I (Cu+) which forms a complex with the nitrogen and carbon of peptide bonds in an alkaline solution. A violet colour indicates the presence of proteins.
Ninhydrin test for amino acid: Ninhydrin (2,2 Dihydroxy indane-l,3-dione) is a chemical used to detect ammonia or primary and secondary amines. When reacting with these free amines, a deep blue or purple colour known as Ruhemann’s purple is evolved. Amino acid analysis of proteins is also done by ninhydrine. Most of the amino acids (including a-amino acids) are hydrolysed and reacted with ninhydrin except proline (a secondary amine). Amino acid containing a free amino group and a free carboxylic acid group reacts together with ninhydrin to produce coloured product. When the amino group is secondary, the condensation product is yellow.
Download our AppSolubility test for fats and oils : A positive solubility test for fats is that the fat dissolves in lighter fluid and not in water. In this test, 5 drops of fat or oil are added in two test tubes containing 10 drops of lighter fluid and 10 drops cold water respectively.
Fruit juice contains sugar so it cannot be tested by the above mentioned tests. Saliva contains proteins, mineral salts, amylase etc., so it can be tested for protein and amino acids. Urine contains proteins, so it can be tested for it.
Question 14: Find out how much cellulose is made by all the plants in the biosphere and compare it with how much of paper is manufactured by man and hence what is the consumption of plant material by man annually. What a loss of vegetation!
Answer Approximately, 100 billion tonnes of cellulose are made per year by all the plants in the biosphere and it takes 17 full grown trees to make one ton of paper. Trees are also used to fulfil the other requirements of man such as for timber, food, medicines, etc. Hence, it is difficult to calculate the annual consumption of plant material by
man.
Answer Approximately, 100 billion tonnes of cellulose are made per year by all the plants in the biosphere and it takes 17 full grown trees to make one ton of paper. Trees are also used to fulfil the other requirements of man such as for timber, food, medicines, etc. Hence, it is difficult to calculate the annual consumption of plant material by
man.
Question 15: Describe the important properties of enzymes.
Answer Properties of enzymes
(1) Enzymes are complex macromolecules with high molecular weight.
(2) They catalyze biochemical reactions in a cell. They help in the breakdown of
large molecules into smaller molecules or bring together two smaller molecules to
form a larger molecule.
(3) Enzymes do not start a reaction. However, they help in accelerating it.
(4) Enzymes affect the rate of biochemical reaction and not the direction.
(5) Most of the enzymes have high turnover number. Turnover number of an enzyme is the number of molecules of a substance that is acted upon by an enzyme per minute. High turnover number of enzymes increases the efficiency of reaction.
(6) Enzymes are specific in action.
(7) Enzymatic activity decreases with increase in temperature.
(8) They show maximum activity at an optimum pH of 6 – 8.
(9) The velocity of enzyme increases with increase in substrate concentration and then, ultimately reaches maximum velocity.
Answer Properties of enzymes
(1) Enzymes are complex macromolecules with high molecular weight.
(2) They catalyze biochemical reactions in a cell. They help in the breakdown of
large molecules into smaller molecules or bring together two smaller molecules to
form a larger molecule.
(3) Enzymes do not start a reaction. However, they help in accelerating it.
(4) Enzymes affect the rate of biochemical reaction and not the direction.
(5) Most of the enzymes have high turnover number. Turnover number of an enzyme is the number of molecules of a substance that is acted upon by an enzyme per minute. High turnover number of enzymes increases the efficiency of reaction.
(6) Enzymes are specific in action.
(7) Enzymatic activity decreases with increase in temperature.
(8) They show maximum activity at an optimum pH of 6 – 8.
(9) The velocity of enzyme increases with increase in substrate concentration and then, ultimately reaches maximum velocity.
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